Abstract
Ubiquitination is known to be important for endocytosis and lysosomal degradation of aquaporin-2 (AQP2). Ubiquitin (Ub) is covalently attached to the lysine residue of the substrate proteins and activation and attachment of Ub to a target protein is mediated by the action of three enzymes (i.e., E1, E2, and E3). In particular, E3 Ub-protein ligases are known to have substrate specificity. This minireview will discuss the ubiquitination of AQP2 and identification of potential E3 Ub-protein ligases for 1-deamino-8-D-arginine vasopressin (dDAVP)-dependent AQP2 regulation.
Original language | English |
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Pages (from-to) | 1-4 |
Number of pages | 4 |
Journal | Electrolyte and Blood Pressure |
Volume | 7 |
Issue number | 1 |
DOIs | |
State | Published - Jun 2009 |
Keywords
- Aquaporin 2
- Collecting
- Kidney tubules
- Ubiquitination
- Vasopressins